Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2018 Dec 28;47(5):2666–2680. doi: 10.1093/nar/gky1299

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

PMC Copyright notice

Figure 1. — Domain organization of H-NS. (A) Sequence alignment showing structural elements (α-helices, β-strands; η represents a 3₁₀ helix). Protein domains (determined from experimental structures) are green: N-terminal dimerization domain (site1); blue: central dimerization domain (site2), purple: positively charged linker; yellow: C-terminal DNA binding domain (DNAbd). Positions of S. typhimurium residues showing chemical shift changes in presence of H-NS_84–137 or H-NS_2–57 are indicated by an asterisk. (B) Schematic structural model for multimerization through site1 (light and dark green) and site2 (light and dark cyan) extracted from the H-NS superhelix conformation (see (35) and PDB 3NR7). The charged linker (purple) and DNAbd (yellow) are not included in the crystallographic model. Dashed square brackets outline the construct used in MD simulations.